Evidence map›Paper›PMID 33508027›Full record

ArticlePLoS pathogens2021

Kaposi's sarcoma-associated herpesvirus processivity factor (PF-8) recruits cellular E3 ubiquitin ligase CHFR to promote PARP1 degradation and lytic replication.

Woo-Chang Chung, Seungrae Lee, Yejin Kim, Jong Bok Seo, Moon Jung Song

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
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  4. TRIM28 drives immune evasion via PARP1 SUMOylation and NADJournal for immunotherapy of cancer · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Woo-Chang ChungVirus-Host Interactions Laboratory, Department of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul, Republic of Korea.ORCID 0000-0003-2264-9065
Seungrae LeeVirus-Host Interactions Laboratory, Department of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul, Republic of Korea.ORCID 0000-0003-3615-3650
Yejin KimVirus-Host Interactions Laboratory, Department of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul, Republic of Korea.ORCID 0000-0002-6388-0071
Jong Bok SeoMetabolome Analysis Team, Korea Basic Science Institute, Seoul, Republic of Korea.ORCID 0000-0003-2058-5045
Moon Jung SongVirus-Host Interactions Laboratory, Department of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul, Republic of Korea.
Korea University · KRKorea Basic Science Institute · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Kaposi's sarcoma-associated herpesvirus (KSHV), which belongs to the gammaherpesvirus subfamily, is associated with the pathogenesis of various tumors. Nuclear enzyme poly(ADP-ribose) polymerase 1 (PARP1) catalyzes the polymerization of ADP-ribose units on target proteins. In KSHV-infected cells, PARP1 inhibits replication and transcription activator (RTA), a molecular switch that initiates lytic replication, through direct interaction. Thus, for efficient replication, KSHV has to overcome the molecular barrier in the form of PARP1. Previously, we have demonstrated that KSHV downregulates the expression of PARP1 through PF-8, a viral processivity factor. PF-8 induces ubiquitin-proteasome system-mediated degradation of PARP1 via direct physical association and enhances RTA transactivation activity. Here, we showed that dimerization domains of PF-8 are crucial not only for PARP1 interaction and degradation but also for enhancement of the RTA transactivation activity. PF-8 recruited CHFR for the PARP1 degradation. A knockdown of CHFR attenuated the PF-8-induced PARP1 degradation and enhancement of the RTA transactivation activity, leading to reduced KSHV lytic replication. These findings reveal a mechanism by which KSHV PF-8 recruits a cellular E3 ligase to curtail the inhibitory effect of PARP1 on KSHV lytic replication.

Indexed as

Cell Cycle ProteinsDimerizationDown-RegulationHerpesvirus 8, HumanHumansImmediate-Early ProteinsNeoplasm ProteinsPoly-ADP-Ribose Binding ProteinsPoly (ADP-Ribose) Polymerase-1Proteasome Endopeptidase ComplexProtein DomainsProteolysisTrans-ActivatorsUbiquitinUbiquitin-Protein LigasesViral ProteinsCell Cycle ProteinsCHFR protein, humanImmediate-Early ProteinsNeoplasm ProteinsORF59 protein, Human herpesvirus 8PARP1 protein, humanPoly-ADP-Ribose Binding ProteinsPoly (ADP-Ribose) Polymerase-1Proteasome Endopeptidase ComplexRta protein, Human herpesvirus 8Trans-ActivatorsUbiquitinUbiquitin-Protein LigasesViral Proteins

Identifiers

PMID33508027
PMCPMC7872283
OpenAlexW3125458845

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.